› 7q8l

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130186 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin L2 Chains: AA, BA
Molecule details ›
Chains: AA, BA
Length: 222 amino acids
Theoretical weight: 24.14 KDa
Source organism: Homo sapiens
Expression system: Komagataella phaffii GS115
UniProt:
  • Canonical: O60911 (Residues: 113-334; Coverage: 70%)
Gene names: CATL2, CTSL2, CTSU, CTSV, UNQ268/PRO305
Sequence domains: Papain family cysteine protease
VPCGTAHE Peptide Chains: PA, PB
Molecule details ›
Chains: PA, PB
Length: 10 amino acids
Theoretical weight: 838 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand MPD 3 x MPD
Ligand CL 2 x CL
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 11.2C
Spacegroup: P43212
Unit cell:
a: 94.35Å b: 94.35Å c: 127.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.167 0.188
Expression systems:
  • Komagataella phaffii GS115
  • Not provided

Quick links

Citations

2 citation in other articles

Calpeptin is a potent cathepsin inhibitor and drug candidate for SARS-CoV-2 infections.
Reinke et al. (2023)
1 more

1 mention without citation

Proteomic data and structure analysis combined reveal interplay of structural rigidity and flexibility on selectivity of cysteine cathepsins.
Tušar et al. (2023)